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The P4‐ATPase Drs2 interacts with and stabilizes the multisubunit tethering complex TRAPPIII in yeast
Multisubunit Tethering Complexes (MTCs) are a set of conserved protein complexes that tether vesicles at the acceptor membrane. Interactions with other components of the trafficking machinery regulate MTCs through mechanisms that are partially understood. Here, we systematically investigate the inte...
Autores principales: | , , , , , , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10157312/ https://www.ncbi.nlm.nih.gov/pubmed/36929574 http://dx.doi.org/10.15252/embr.202256134 |
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author | Pazos, Irene Puig‐Tintó, Marta Betancur, Laura Cordero, Jorge Jiménez‐Menéndez, Nereida Abella, Marc Hernández, Altair C Duran, Ana G Adachi‐Fernández, Emi Belmonte‐Mateos, Carla Sabido‐Bozo, Susana Tosi, Sébastien Nezu, Akiko Oliva, Baldomero Colombelli, Julien Graham, Todd R Yoshimori, Tamotsu Muñiz, Manuel Hamasaki, Maho Gallego, Oriol |
author_facet | Pazos, Irene Puig‐Tintó, Marta Betancur, Laura Cordero, Jorge Jiménez‐Menéndez, Nereida Abella, Marc Hernández, Altair C Duran, Ana G Adachi‐Fernández, Emi Belmonte‐Mateos, Carla Sabido‐Bozo, Susana Tosi, Sébastien Nezu, Akiko Oliva, Baldomero Colombelli, Julien Graham, Todd R Yoshimori, Tamotsu Muñiz, Manuel Hamasaki, Maho Gallego, Oriol |
author_sort | Pazos, Irene |
collection | PubMed |
description | Multisubunit Tethering Complexes (MTCs) are a set of conserved protein complexes that tether vesicles at the acceptor membrane. Interactions with other components of the trafficking machinery regulate MTCs through mechanisms that are partially understood. Here, we systematically investigate the interactome that regulates MTCs. We report that P4‐ATPases, a family of lipid flippases, interact with MTCs that participate in the anterograde and retrograde transport at the Golgi, such as TRAPPIII. We use the P4‐ATPase Drs2 as a paradigm to investigate the mechanism and biological relevance of this interplay during transport of Atg9 vesicles. Binding of Trs85, the sole‐specific subunit of TRAPPIII, to the N‐terminal tail of Drs2 stabilizes TRAPPIII on membranes loaded with Atg9 and is required for Atg9 delivery during selective autophagy, a role that is independent of P4‐ATPase canonical functions. This mechanism requires a conserved I(S/R)TTK motif that also mediates the interaction of the P4‐ATPases Dnf1 and Dnf2 with MTCs, suggesting a broader role of P4‐ATPases in MTC regulation. |
format | Online Article Text |
id | pubmed-10157312 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-101573122023-05-05 The P4‐ATPase Drs2 interacts with and stabilizes the multisubunit tethering complex TRAPPIII in yeast Pazos, Irene Puig‐Tintó, Marta Betancur, Laura Cordero, Jorge Jiménez‐Menéndez, Nereida Abella, Marc Hernández, Altair C Duran, Ana G Adachi‐Fernández, Emi Belmonte‐Mateos, Carla Sabido‐Bozo, Susana Tosi, Sébastien Nezu, Akiko Oliva, Baldomero Colombelli, Julien Graham, Todd R Yoshimori, Tamotsu Muñiz, Manuel Hamasaki, Maho Gallego, Oriol EMBO Rep Articles Multisubunit Tethering Complexes (MTCs) are a set of conserved protein complexes that tether vesicles at the acceptor membrane. Interactions with other components of the trafficking machinery regulate MTCs through mechanisms that are partially understood. Here, we systematically investigate the interactome that regulates MTCs. We report that P4‐ATPases, a family of lipid flippases, interact with MTCs that participate in the anterograde and retrograde transport at the Golgi, such as TRAPPIII. We use the P4‐ATPase Drs2 as a paradigm to investigate the mechanism and biological relevance of this interplay during transport of Atg9 vesicles. Binding of Trs85, the sole‐specific subunit of TRAPPIII, to the N‐terminal tail of Drs2 stabilizes TRAPPIII on membranes loaded with Atg9 and is required for Atg9 delivery during selective autophagy, a role that is independent of P4‐ATPase canonical functions. This mechanism requires a conserved I(S/R)TTK motif that also mediates the interaction of the P4‐ATPases Dnf1 and Dnf2 with MTCs, suggesting a broader role of P4‐ATPases in MTC regulation. John Wiley and Sons Inc. 2023-03-16 /pmc/articles/PMC10157312/ /pubmed/36929574 http://dx.doi.org/10.15252/embr.202256134 Text en © 2023 The Authors. Published under the terms of the CC BY NC ND 4.0 license https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc-nd/4.0/ (https://creativecommons.org/licenses/by-nc-nd/4.0/) License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made. |
spellingShingle | Articles Pazos, Irene Puig‐Tintó, Marta Betancur, Laura Cordero, Jorge Jiménez‐Menéndez, Nereida Abella, Marc Hernández, Altair C Duran, Ana G Adachi‐Fernández, Emi Belmonte‐Mateos, Carla Sabido‐Bozo, Susana Tosi, Sébastien Nezu, Akiko Oliva, Baldomero Colombelli, Julien Graham, Todd R Yoshimori, Tamotsu Muñiz, Manuel Hamasaki, Maho Gallego, Oriol The P4‐ATPase Drs2 interacts with and stabilizes the multisubunit tethering complex TRAPPIII in yeast |
title | The
P4‐ATPase
Drs2 interacts with and stabilizes the multisubunit tethering complex
TRAPPIII
in yeast |
title_full | The
P4‐ATPase
Drs2 interacts with and stabilizes the multisubunit tethering complex
TRAPPIII
in yeast |
title_fullStr | The
P4‐ATPase
Drs2 interacts with and stabilizes the multisubunit tethering complex
TRAPPIII
in yeast |
title_full_unstemmed | The
P4‐ATPase
Drs2 interacts with and stabilizes the multisubunit tethering complex
TRAPPIII
in yeast |
title_short | The
P4‐ATPase
Drs2 interacts with and stabilizes the multisubunit tethering complex
TRAPPIII
in yeast |
title_sort |
p4‐atpase
drs2 interacts with and stabilizes the multisubunit tethering complex
trappiii
in yeast |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10157312/ https://www.ncbi.nlm.nih.gov/pubmed/36929574 http://dx.doi.org/10.15252/embr.202256134 |
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